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ENPP2 (ectonucleotide pyrophosphatase/phosphodiesterase 2)

Identity

Other namesAutotaxin
ATX
NPP2
PD1alpha
lysophospholipase D
PDNP2
HGNC (Hugo) ENPP2
LocusID (NCBI) 5168
Location 8q24.12
Location_base_pair Starts at 120569317 and ends at 120651106 bp from pter ( according to hg19-Feb_2009)  [Mapping]
Local_order Telomeric to NOV (nephroblastoma overxpressed gene), centromeric to TAF2; colocalized with pseudogene CYCSP23.

DNA/RNA

Note mRNA length 3276 or 3120 bp, depending upon alternate splicing.
 
  ENPP2 Gene: Intron-exon organization of ENPP2.
Description The ENPP2 gene is 81,754 bp in length and is composed of 26 exons. Part of exon 1 and 26 are untranslated (UTR); translation extends from the remainder of exon 1 through the proximal portion of exon 26; however, there is a 152 bp exon (exon 12) that is alternatively spliced and is included primarily in neurally derived tissues.
Transcription The mRNA for ENPP2 is 3276 bp with exon 12 and 3120 bp without it. The ENPP2 promoter is reported to have four SP1 sites as well as binding sites for NFAT and NF-kappaB but no TATA or CAAT boxes. The only transcription factor that has been proven to increase ENPP2 protein expression is NFATC2/NFAT1, after release of alpha6beta4 from hemidesmosomes in a breast cancer cell line. A number of growth factors have been found to stimulate ENPP2 protein expression, while several inflammatory cytokines have been reported to inhibit expression.
Pseudogene CYCSP23

Protein

 
  ENPP2 Protein (NPP2/ATX): Organization of domains and other critical elements within ENPP2.
Description The ENPP2 protein, NPP2 or ATX, is an N-glycolsylated member of the ecto-nucleotide pyrophosphatase and phosphodiesterase (NPP) family of proteins. The NPP2 precursor contains 915 amino acids, 105.2 KDa; and an alternately spliced variant is 863 amino acids, 99.0 KDa. The amino terminal signal peptide sequence is cleaved at a signal peptidase site between G27 and F28 to yield a secreted protein that contains 888/836 amino acids, 102.3/96.9 KDa. NPP2 contains up to 3 ASN-linked glycosylation sites that appear to be required for secretion as well as for stabilization of its active conformation.
Expression NPP2 is expressed in many tissues during development, but it is critical for blood vessel maturation and neurogenesis. Certain inflammatory cytokines and the tumor suppressor CST6 downregulate ENPP2 expression, and some of the NPP2 products exert a negative feedback on its expression. Conversely, a number of growth factors as well as EBV infection (in Hodgkin's lymphoma) upregulate ENPP2 expression. Disruption of hemidesmosomes in breast cancer cells releases alpha6beta4, which initiates a signaling cascade that culminates in the activation of the transcription factor NFAT1, which binds to the ENPP2 promoter to upregulate protein expression. Upregulation of ENPP2 has been reported in a number of aggressive tumors, including glioblastoma, undifferentiated anaplastic thyroid carcinoma, invasive breast carcinoma, and metastatic hepatocellular carcinoma.
In adults, NPP2 is the major source of serum and plasma lysophospholipase D activity. It is also highly expressed in brain, kidney, liver, ovary, small intestine, and placenta, and is present in many other tissues.
Function NPP2 is a Type 2 nucleotide pyrophosphatase and phosphodiesterase that also has ATPase activity. In addition, NPP2 is the major source of serum and plasma lysophospholipase D activity, hydrolyzing lysophosphatidylcholine into lysophosphatidic acid as well as cyclic phosphatidic acid. NPP2 also hydrolyzes sphingosylphosphorylcholine into sphingosine-1-phosphate; however, NPP2 is not a major source of sphingosine-1-phosphate in plasma. The production of lysophosphatidic acid is thought to account for many of the physiological and pathological roles of ENPP2.
Both enzymatic activities of NPP2 share a common catalytic domain. Like other members of the NPP family, NPP2 is a metallo-enzyme with binding sites for 2 metal atoms coordinated by three critical histidines (H316, H360, and H475) and associated aspartates (D172, D312, and D359). T210 is nucleotidylated during the nucleotide pyrophosphatase/phosphodiesterase reaction and is essential for hydrolysis of substrate during the lysophospholipase D reaction as well.
Homology NPP2 is a member of the nucleotide pyrophosphatase and phosphodiesterase family, which includes ENPP1 (PC1) and ENPP3 (B10). Although the catalytic domain is highly conserved within this family of proteins, only NPP2 possesses lysophospholipase D activity.

Mutations

Note There are a number of single nucleotide polymorphisms (SNPs) that have been reported within the ENPP2 gene but none are yet reported to be associated with altered phenotype. However, knockout of ENPP2 is lethal in mice (approximately E12), therefore mutations associated with loss of function might be lethal.

Implicated in

Entity Various cancers
Disease Overexpression of the ENPP2 protein has been associated with tumor cell motility and invasion, tumor growth and metastasis, and blood vessel formation.
Prognosis ENPP2 is over-expressed in poorly differentiated non-small cell lung carcinomas and invasive and metastatic hepatocellular carcinoma. In thyroid carcinomas, ENPP2 expression was found to be higher in undifferentiated anaplastic thyroid carcinoma cell lines and tissues than in follicular thyroid carcinomas or goiters. When glioblastoma multiforme cells were collected from tumor cores vs. areas of white matter invasion, ENPP2 was found to be overexpressed predominantly at the invasive front.
Oncogenesis Upregulation of NPP2 expression appears to be associated with cancer progression rather than with oncogenesis. Transfection of ENPP2 cDNA into mouse fibroblast cell lines (NIH3T3 clone7) did not result in tumorigenic cell lines, but transfection into Ras-transformed fibroblasts resulted in rapidly growing, hematogenous, highly metastatic tumors. NPP2 expression was found in Hodgkin's lymphoma cells as well as in CD30+ anaplastic large-cell lymphomas. In the Hodgkin's lymphomas , EBV infection was correlated to induction of ENPP2 expression (P = 0.006).
Transfection of the tumor suppressor CST6 into MDA-MB-435 cells resulted in down-regulation of ENPP2. In contrast, down regulation of ENPP2 by specific siRNAs resulted in down-regulation of the tumor suppressors, thrombospondin-1 and thrombospondin-2 (THBS1 and THBS2, respectively).
  
Entity Diabetes
Disease NPP2 expression is highly upregulated during adipocyte differentiation and its product, lysophosphatidic acid, stimulates proliferation in preadipocytes. In genetically obese, diabetic mice, NPP2 expression was increased in adipose tissue compared to their lean siblings. This is a possible model for type 2 diabetes, which has a strong genetic component.
  

External links

Nomenclature
HGNC (Hugo)ENPP2   3357
Cards
AtlasENPP2ID40455ch8q24
Entrez_Gene (NCBI)ENPP2  5168  ectonucleotide pyrophosphatase/phosphodiesterase 2
GeneCards (Weizmann)ENPP2
Ensembl (Hinxton)ENSG00000136960 [Gene_View]  chr8:120569317-120651106 [Contig_View]  ENPP2 [Vega]
ICGC DataPortalENSG00000136960
AceView (NCBI)ENPP2
Genatlas (Paris)ENPP2
WikiGenes5168
SOURCE (Princeton)NM_001040092 NM_001130863 NM_006209
Genomic and cartography
GoldenPath (UCSC)ENPP2  -  8q24.12   chr8:120569317-120651106 -  8q24.1   [Description]    (hg19-Feb_2009)
EnsemblENPP2 - 8q24.1 [CytoView]
Mapping of homologs : NCBIENPP2 [Mapview]
OMIM601060   
Gene and transcription
Genbank (Entrez)AA256687 AI339551 AI375195 AK124910 AK130313
RefSeq transcript (Entrez)NM_001040092 NM_001130863 NM_006209
RefSeq genomic (Entrez)AC_000140 NC_000008 NC_018919 NG_029498 NT_008046 NW_001839136 NW_004929340
Consensus coding sequences : CCDS (NCBI)ENPP2
Cluster EST : UnigeneHs.190977 [ NCBI ]
CGAP (NCI)Hs.190977
Alternative Splicing : Fast-db (Paris)GSHG0029815
Alternative Splicing GalleryENSG00000136960
Gene ExpressionENPP2 [ NCBI-GEO ]     ENPP2 [ SEEK ]   ENPP2 [ MEM ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ13822 (Uniprot)
NextProtQ13822  [Medical]
With graphics : InterProQ13822
Splice isoforms : SwissVarQ13822 (Swissvar)
Catalytic activity : Enzyme3.1.4.39 [ Enzyme-Expasy ]   3.1.4.393.1.4.39 [ IntEnz-EBI ]   3.1.4.39 [ BRENDA ]   3.1.4.39 [ KEGG ]   
Domaine pattern : Prosite (Expaxy)SMB_1 (PS00524)    SMB_2 (PS50958)   
Domains : Interpro (EBI)Alkaline_Pase-like_a/b/a    Alkaline_phosphatase_core    DNA/RNA_non-sp_Endonuclease    E-NPP    Extracellular_endonuc_su_A    Phosphodiest/P_Trfase    Somatomedin_B_chordata    Somatomedin_B_dom   
Related proteins : CluSTrQ13822
Domain families : Pfam (Sanger)Endonuclease_NS (PF01223)    Phosphodiest (PF01663)    Somatomedin_B (PF01033)   
Domain families : Pfam (NCBI)pfam01223    pfam01663    pfam01033   
Domain families : Smart (EMBL)Endonuclease_NS (SM00892)  NUC (SM00477)  SO (SM00201)  
DMDM Disease mutations5168
Blocks (Seattle)Q13822
Human Protein AtlasENSG00000136960
Peptide AtlasQ13822
HPRD03037
IPIIPI00156171   IPI00303210   IPI00878576   IPI00980017   IPI00977592   IPI01008796   IPI00983728   IPI00794024   
Protein Interaction databases
DIP (DOE-UCLA)Q13822
IntAct (EBI)Q13822
FunCoupENSG00000136960
BioGRIDENPP2
IntegromeDBENPP2
STRING (EMBL)ENPP2
Ontologies - Pathways
QuickGOQ13822
Ontology : AmiGOnucleic acid binding  phosphodiesterase I activity  nucleotide diphosphatase activity  lysophospholipase activity  scavenger receptor activity  calcium ion binding  extracellular space  extracellular space  plasma membrane  integral component of plasma membrane  phosphate-containing compound metabolic process  receptor-mediated endocytosis  cellular component movement  chemotaxis  immune response  G-protein coupled receptor signaling pathway  transcription factor binding  zinc ion binding  phospholipid catabolic process  hydrolase activity  polysaccharide binding  regulation of cell migration  phosphatidylcholine catabolic process  alkylglycerophosphoethanolamine phosphodiesterase activity  nucleic acid phosphodiester bond hydrolysis  
Ontology : EGO-EBInucleic acid binding  phosphodiesterase I activity  nucleotide diphosphatase activity  lysophospholipase activity  scavenger receptor activity  calcium ion binding  extracellular space  extracellular space  plasma membrane  integral component of plasma membrane  phosphate-containing compound metabolic process  receptor-mediated endocytosis  cellular component movement  chemotaxis  immune response  G-protein coupled receptor signaling pathway  transcription factor binding  zinc ion binding  phospholipid catabolic process  hydrolase activity  polysaccharide binding  regulation of cell migration  phosphatidylcholine catabolic process  alkylglycerophosphoethanolamine phosphodiesterase activity  nucleic acid phosphodiester bond hydrolysis  
Pathways : KEGGEther lipid metabolism   
Protein Interaction DatabaseENPP2
Wikipedia pathwaysENPP2
Gene fusion - rearrangments
Polymorphisms : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)ENPP2
SNP (GeneSNP Utah)ENPP2
SNP : HGBaseENPP2
Genetic variants : HAPMAPENPP2
1000_GenomesENPP2 
ICGC programENSG00000136960 
CONAN: Copy Number AnalysisENPP2 
Somatic Mutations in Cancer : COSMICENPP2 
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
DECIPHER (Syndromes)8:120569317-120651106
Mutations and Diseases : HGMDENPP2
OMIM601060   
MedgenENPP2
GENETestsENPP2
Disease Genetic AssociationENPP2
Huge Navigator ENPP2 [HugePedia]  ENPP2 [HugeCancerGEM]
Genomic VariantsENPP2  ENPP2 [DGVbeta]
Exome VariantENPP2
dbVarENPP2
ClinVarENPP2
snp3D : Map Gene to Disease5168
General knowledge
Homologs : HomoloGeneENPP2
Homology/Alignments : Family Browser (UCSC)ENPP2
Phylogenetic Trees/Animal Genes : TreeFamENPP2
Chemical/Protein Interactions : CTD5168
Chemical/Pharm GKB GenePA27792
Clinical trialENPP2
Cancer Resource (Charite)ENSG00000136960
Other databases
Probes
Litterature
PubMed98 Pubmed reference(s) in Entrez
CoreMineENPP2
GoPubMedENPP2
iHOPENPP2

Bibliography

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cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases.
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PMID 10645002
 
Structural and catalytic similarities between nucleotide pyrophosphatases/phosphodiesterases and alkaline phosphatases.
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PMID 11027689
 
Autotaxin (NPP-2), a metastasis-enhancing motogen, is an angiogenic factor.
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PMID 11559573
 
Autotaxin promotes motility via G protein-coupled phosphoinositide 3-kinase gamma in human melanoma cells.
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Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase.
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PMID 12119361
 
Expression of autotaxin (NPP-2) is closely linked to invasiveness of breast cancer cells.
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PMID 12498389
 
Autotaxin hydrolyzes sphingosylphosphorylcholine to produce the regulator of migration, sphingosine-1-phosphate.
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PMID 14500380
 
Autotaxin is released from adipocytes, catalyzes lysophosphatidic acid synthesis, and activates preadipocyte proliferation. Up-regulated expression with adipocyte differentiation and obesity.
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Site-directed mutations in the tumor-associated cytokine, autotaxin, eliminate nucleotide phosphodiesterase, lysophospholipase D, and motogenic activities.
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Microarray analysis identifies Autotaxin, a tumour cell motility and angiogenic factor with lysophospholipase D activity, as a specific target of cell transformation by v-Jun.
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Autotaxin stimulates urokinase-type plasminogen activator expression through phosphoinositide 3-kinase-Akt-nuclear [corrected] factor kappa B signaling cascade in human melanoma cells.
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Autotaxin stabilizes blood vessels and is required for embryonic vasculature by producing lysophosphatidic acid.
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Cyclic phosphatidic acid is produced by autotaxin in blood.
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Autotaxin, a secreted lysophospholipase D, is essential for blood vessel formation during development.
van Meeteren LA, Ruurs P, Stortelers C, Bouwman P, van Rooijen MA, Pradąģre JP, Pettit TR, Wakelam MJ, Saulnier-Blache JS, Mummery CL, Moolenaar WH, Jonkers J
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Secretion and lysophospholipase D activity of autotaxin by adipocytes are controlled by N-glycosylation and signal peptidase.
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Autotaxin (NPP-2) in the brain: cell type-specific expression and regulation during development and after neurotrauma.
Savaskan NE, Rocha L, Kotter MR, Baer A, Lubec G, van Meeteren LA, Kishi Y, Aoki J, Moolenaar WH, Nitsch R, Brąßuer AU
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Contributor(s)

Written02-2007Mary L. Stracke, Timothy Clair

Citation

This paper should be referenced as such :
Clair, T ; Stracke, ML
ENPP2 (ectonucleotide pyrophosphatase/phosphodiesterase 2)
Atlas Genet Cytogenet Oncol Haematol. 2007;11(3):182-185.
Free online version   Free pdf version   [Bibliographic record ]
URL : http://AtlasGeneticsOncology.org/Genes/ENPP2ID40455ch8q24.html

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